The presence of cellular aggregates is a hallmark of many neurodegenerative diseases like Alzheimer's Disease, Huntington's Disease and Prion diseases. Recent studies have revealed that the localization of glutamine-rich proteins into aggregates leads to a loss-of-function and is likely the reason for the observed cell toxicity. Cellular aggregates have been associated with the yeast prion [PSI+], a misfolded self-perpetuating form of the SUP35 protein. It appears that the presence of [PSI+] leads to slower growth in some SAGA mutants. Members of the SAGA complex, in conjunction with the Swi/Snf complex and the srb/mediator complex, are involved in chromatin remodeling and co-activation of transcription. Here, it is proposed that in the presence of [PSI+], glutamine rich proteins involved in chromatin remodeling are being recruited to aggregates, which leads to a loss of their function. The effects other yeast prions and variant strains of prions have on SAGA mutants will be tested. In addition, proteins found within cellular aggregates will be identified. The identification of proteins found within aggregate will provide insight to etiology of prion diseases. [unreadable] [unreadable]